OXDC_ARTBC
ID OXDC_ARTBC Reviewed; 425 AA.
AC D4B179;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Oxalate decarboxylase ARB_02208 {ECO:0000250|UniProtKB:O34714};
DE EC=4.1.1.2 {ECO:0000250|UniProtKB:O34714};
DE Flags: Precursor;
GN ORFNames=ARB_02208;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000312|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
CC -!- FUNCTION: Converts oxalate to formate and CO(2) in an O(2)-dependent
CC reaction. Can also catalyze minor side reactions: oxalate oxidation to
CC produce H(2)O(2), and oxalate-dependent, H(2)O(2)-independent dye
CC oxidations. {ECO:0000250|UniProtKB:O34714}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxalate = CO2 + formate; Xref=Rhea:RHEA:16509,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:30623; EC=4.1.1.2;
CC Evidence={ECO:0000250|UniProtKB:O34714};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O34714};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:O34714};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
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DR EMBL; ABSU01000025; EFE31014.1; -; Genomic_DNA.
DR RefSeq; XP_003011654.1; XM_003011608.1.
DR AlphaFoldDB; D4B179; -.
DR SMR; D4B179; -.
DR STRING; 663331.D4B179; -.
DR EnsemblFungi; EFE31014; EFE31014; ARB_02208.
DR GeneID; 9523425; -.
DR KEGG; abe:ARB_02208; -.
DR eggNOG; ENOG502RJG4; Eukaryota.
DR HOGENOM; CLU_030515_2_1_1; -.
DR OMA; WHTNDEW; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046564; F:oxalate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0033609; P:oxalate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR017774; Bicupin_oxalate_deCO2ase/Oxase.
DR InterPro; IPR006045; Cupin_1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF00190; Cupin_1; 2.
DR SMART; SM00835; Cupin_1; 2.
DR SUPFAM; SSF51182; SSF51182; 1.
DR TIGRFAMs; TIGR03404; bicupin_oxalic; 1.
PE 1: Evidence at protein level;
KW Decarboxylase; Glycoprotein; Lyase; Manganese; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..425
FT /note="Oxalate decarboxylase ARB_02208"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434495"
FT DOMAIN 73..236
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 270..414
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT ACT_SITE 378
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 116
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 118
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 122
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 161
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 317
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 319
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 324
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 363
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 425 AA; 46382 MW; A2C819E77D68B146 CRC64;
MKFGSALVAA VAAVAGVAAK DYGGVPGQPI QKSGKGAVFS GATNPQLDLQ NPSNINGQPA
TDIGLVPNLK WSFSLSKTRM FHGGWIREQV ISDLPASHDI AGAQVHLTKG GIRQMHWHRV
AEWGYVYAGS ILVFAVTEDG QYQIDKLTPG DIYYFPKGAA HSFQGIEDEN EVLVAFDEGD
FDKIGYLFPP YYSNINLQLS NAFNYRTTFQ VAEWIAHTPQ DVLAKNFNIS TGGTFDKTKS
NMLEIINSTT STHNVTGPNG ALMGNSSYTF HIRDAPEIQV PGGGGTIQIV DSKNFPISKT
IACAIVRLKP GALRELHWHP TAEEWLYFHS GNARATVYVS GGLSRTFDFT AGDTGVFPDN
AGHYIENVSE DEDLVYLELY KADRVADVSL SQWLALTPHD IAAAAINVPI DVIDKLKKDK
QYIIQ
